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The Charge-State and Structural Stability of Peptides Conferred by Microsolvating Environments in Differential
Christian Ieritano1, Daniel Rickert1, Joshua Featherstone1
1Department of Chemistry, University of Waterloo, 200 University Avenue West, Waterloo N2L 3G1, Ontario, Canada.
Adding solvent vapor to differential mobility spectrometry (DMS) prevents peptide fragmentation by creating a protective microsolvation environment. This "solvent airbag" effect stabilizes ions, reducing temperature and preserving native structures during analysis.
Area of Science:
- Analytical Chemistry
- Physical Chemistry
- Biochemistry
Background:
- Field-induced heating in differential mobility spectrometry (DMS) can cause fragmentation of sensitive analytes like peptides.
- Protonated peptides are susceptible to collisional activation and dissociation within the DMS cell.
- Mitigating fragmentation is crucial for accurate peptide analysis and structural preservation.
Purpose of the Study:
- To investigate the protective effect of solvent vapor microsolvation in DMS on peptide stability.
- To model the microsolvation behavior of protonated amines with various gas-phase modifiers.
- To quantify the temperature reduction and stabilization effects of microsolvation on peptides.
Main Methods:
- Differential mobility spectrometry (DMS) experiments with carrier gas seeded with solvent vapors (H2O, MeOH, EtOH, iPrOH, acetone, MeCN).
- Analysis of protonated peptides (GGG, AAA, Polybia-MP1) and a model amine (n-propylamine).
- Computational modeling of microsolvation propensity and ion temperatures using a modified two-temperature theory.
Main Results:
- Seeding DMS with solvent vapor effectively prevented field-induced fragmentation of protonated peptides.
- All tested solvent molecules formed stable clusters at the protonation sites, acting as a microsolvation shell.
- Microsolvated ions experienced up to 86 K lower effective temperatures, attributed to increased collision cross-section and evaporative cooling.
- Protic solvents facilitated proton abstraction from multiply charged peptides due to enhanced gas-phase basicity and hydrogen-bonding.
Conclusions:
- Microsolvation in DMS acts as a protective 'air bag' for peptides, mitigating field-induced heating and fragmentation.
- This stabilization mechanism preserves charge density and may help maintain native-like peptide conformations.
- Solvent vapor seeding is a viable strategy to enhance the analysis of fragile biomolecules by DMS.
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